ID   PY2CR_COLP3             Reviewed;         316 AA.
AC   Q485R8;
DT   04-MAR-2015, integrated into UniProtKB/Swiss-Prot.
DT   13-SEP-2005, sequence version 1.
DT   03-AUG-2022, entry version 93.
DE   RecName: Full=Delta(1)-pyrroline-2-carboxylate reductase {ECO:0000303|PubMed:24649405};
DE            Short=Pyr2C reductase {ECO:0000303|PubMed:24649405};
DE            EC=1.5.1.49 {ECO:0000269|PubMed:24649405, ECO:0000269|PubMed:24980702};
DE   AltName: Full=Proline ketimine reductase {ECO:0000303|PubMed:24980702};
GN   Name=lhpI {ECO:0000303|PubMed:24649405};
GN   OrderedLocusNames=CPS_1455 {ECO:0000312|EMBL:AAZ26871.1};
OS   Colwellia psychrerythraea (strain 34H / ATCC BAA-681) (Vibrio
OS   psychroerythus).
OC   Bacteria; Proteobacteria; Gammaproteobacteria; Alteromonadales;
OC   Colwelliaceae; Colwellia.
OX   NCBI_TaxID=167879;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=34H / ATCC BAA-681;
RX   PubMed=16043709; DOI=10.1073/pnas.0504766102;
RA   Methe B.A., Nelson K.E., Deming J.W., Momen B., Melamud E., Zhang X.,
RA   Moult J., Madupu R., Nelson W.C., Dodson R.J., Brinkac L.M.,
RA   Daugherty S.C., Durkin A.S., DeBoy R.T., Kolonay J.F., Sullivan S.A.,
RA   Zhou L., Davidsen T.M., Wu M., Huston A.L., Lewis M., Weaver B.,
RA   Weidman J.F., Khouri H., Utterback T.R., Feldblyum T.V., Fraser C.M.;
RT   "The psychrophilic lifestyle as revealed by the genome sequence of
RT   Colwellia psychrerythraea 34H through genomic and proteomic analyses.";
RL   Proc. Natl. Acad. Sci. U.S.A. 102:10913-10918(2005).
RN   [2]
RP   FUNCTION, CATALYTIC ACTIVITY, SUBUNIT, AND BIOPHYSICOCHEMICAL PROPERTIES.
RC   STRAIN=34H / ATCC BAA-681;
RX   PubMed=24649405; DOI=10.1016/j.fob.2014.02.010;
RA   Watanabe S., Tanimoto Y., Yamauchi S., Tozawa Y., Sawayama S., Watanabe Y.;
RT   "Identification and characterization of trans-3-hydroxy-L-proline
RT   dehydratase and Delta(1)-pyrroline-2-carboxylate reductase involved in
RT   trans-3-hydroxy-L-proline metabolism of bacteria.";
RL   FEBS Open Bio 4:240-250(2014).
RN   [3]
RP   FUNCTION, CATALYTIC ACTIVITY, AND BIOPHYSICOCHEMICAL PROPERTIES.
RX   PubMed=24980702; DOI=10.7554/elife.03275;
RA   Zhao S., Sakai A., Zhang X., Vetting M.W., Kumar R., Hillerich B.,
RA   San Francisco B., Solbiati J., Steves A., Brown S., Akiva E., Barber A.,
RA   Seidel R.D., Babbitt P.C., Almo S.C., Gerlt J.A., Jacobson M.P.;
RT   "Prediction and characterization of enzymatic activities guided by sequence
RT   similarity and genome neighborhood networks.";
RL   Elife 3:E03275-E03275(2014).
CC   -!- FUNCTION: Catalyzes the reduction of Delta(1)-pyrroline-2-carboxylate
CC       (Pyr2C) to L-proline, using preferentially NADPH over NADH as the
CC       electron donor. Together with LhpH, is involved in a metabolic pathway
CC       that converts trans-3-hydroxy-L-proline (t3LHyp) to L-proline. To a
CC       much lesser extent, can also reduce Delta(1)-piperideine-2-carboxylate
CC       (Pip2C) to L-pipecolate in vitro; however, this activity has likely no
CC       physiological significance in vivo since C.psychrerythraea probably
CC       possesses no ability to metabolize D-lysine via the L-pipecolate
CC       pathway. Does not show ornithine cyclodeaminase (OCD) activity.
CC       {ECO:0000269|PubMed:24649405, ECO:0000269|PubMed:24980702}.
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=L-proline + NAD(+) = 1-pyrroline-2-carboxylate + H(+) + NADH;
CC         Xref=Rhea:RHEA:20321, ChEBI:CHEBI:15378, ChEBI:CHEBI:39785,
CC         ChEBI:CHEBI:57540, ChEBI:CHEBI:57945, ChEBI:CHEBI:60039; EC=1.5.1.49;
CC         Evidence={ECO:0000269|PubMed:24649405, ECO:0000269|PubMed:24980702};
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=L-proline + NADP(+) = 1-pyrroline-2-carboxylate + H(+) +
CC         NADPH; Xref=Rhea:RHEA:20317, ChEBI:CHEBI:15378, ChEBI:CHEBI:39785,
CC         ChEBI:CHEBI:57783, ChEBI:CHEBI:58349, ChEBI:CHEBI:60039; EC=1.5.1.49;
CC         Evidence={ECO:0000269|PubMed:24649405, ECO:0000269|PubMed:24980702};
CC   -!- BIOPHYSICOCHEMICAL PROPERTIES:
CC       Kinetic parameters:
CC         KM=5.90 mM for Delta(1)-pyrroline-2-carboxylate (using NADPH, at pH
CC         6.5) {ECO:0000269|PubMed:24649405};
CC         KM=2.79 mM for Delta(1)-pyrroline-2-carboxylate (using NADH, at pH
CC         6.5) {ECO:0000269|PubMed:24649405};
CC         KM=7.26 mM for Delta(1)-piperideine-2-carboxylate (using NADPH, at pH
CC         6.5) {ECO:0000269|PubMed:24649405};
CC         KM=2.10 mM for Delta(1)-piperideine-2-carboxylate (using NADH, at pH
CC         6.5) {ECO:0000269|PubMed:24649405};
CC         KM=8.28 mM for Delta(1)-pyrroline-(4S)-hydroxy-2-carboxylate (using
CC         NADPH, at pH 6.5) {ECO:0000269|PubMed:24649405};
CC         KM=18.3 mM for L-proline (using NADP(+), at pH 10.5)
CC         {ECO:0000269|PubMed:24649405};
CC         KM=18.8 mM for L-proline (using NAD(+), at pH 10.5)
CC         {ECO:0000269|PubMed:24649405};
CC         KM=80.1 mM for L-pipecolate (using NADP(+), at pH 10.5)
CC         {ECO:0000269|PubMed:24649405};
CC         KM=1.8 mM for Delta(1)-pyrroline-2-carboxylate (using NADPH as
CC         cosubstrate) {ECO:0000269|PubMed:24980702};
CC         Note=kcat is 7470 min(-1) for Pyr2C reduction using NADPH. kcat is
CC         621 min(-1) for Pyr2C reduction using NADH. kcat is 82.0 min(-1) for
CC         Pip2C reduction using NADPH. kcat is 5.27 min(-1) for Pip2C reduction
CC         using NADH. kcat is 61.3 min(-1) for Delta(1)-pyrroline-(4S)-hydroxy-
CC         2-carboxylate (Pyr4SH2C) reduction using NADPH. kcat is 65.3 min(-1)
CC         for L-proline oxidation using NADP(+). kcat is 0.415 min(-1) for L-
CC         proline oxidation using NAD(+). kcat is 1.28 min(-1) for L-pipecolate
CC         oxidation using NADP(+). {ECO:0000269|PubMed:24649405};
CC       pH dependence:
CC         Optimum pH is 6.5 for Pyr2C reduction and 10.5 for L-proline
CC         oxidation. {ECO:0000269|PubMed:24649405};
CC   -!- SUBUNIT: Homodimer. {ECO:0000269|PubMed:24649405}.
CC   -!- SIMILARITY: Belongs to the ornithine cyclodeaminase/mu-crystallin
CC       family. {ECO:0000305|PubMed:24649405}.
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DR   EMBL; CP000083; AAZ26871.1; -; Genomic_DNA.
DR   RefSeq; WP_011042291.1; NC_003910.7.
DR   AlphaFoldDB; Q485R8; -.
DR   SMR; Q485R8; -.
DR   STRING; 167879.CPS_1455; -.
DR   DNASU; 3521126; -.
DR   EnsemblBacteria; AAZ26871; AAZ26871; CPS_1455.
DR   KEGG; cps:CPS_1455; -.
DR   eggNOG; COG2423; Bacteria.
DR   HOGENOM; CLU_042088_1_2_6; -.
DR   OMA; VGLPWQD; -.
DR   OrthoDB; 1193876at2; -.
DR   BRENDA; 1.5.1.1; 8143.
DR   SABIO-RK; Q485R8; -.
DR   Proteomes; UP000000547; Chromosome.
DR   GO; GO:0016491; F:oxidoreductase activity; IEA:UniProtKB-KW.
DR   Gene3D; 3.30.1780.10; -; 1.
DR   InterPro; IPR036291; NAD(P)-bd_dom_sf.
DR   InterPro; IPR003462; ODC_Mu_crystall.
DR   InterPro; IPR023401; ODC_N.
DR   PANTHER; PTHR13812; PTHR13812; 1.
DR   Pfam; PF02423; OCD_Mu_crystall; 1.
DR   PIRSF; PIRSF001439; CryM; 1.
DR   SUPFAM; SSF51735; SSF51735; 1.
PE   1: Evidence at protein level;
KW   NAD; NADP; Oxidoreductase; Reference proteome.
FT   CHAIN           1..316
FT                   /note="Delta(1)-pyrroline-2-carboxylate reductase"
FT                   /id="PRO_0000432296"
SQ   SEQUENCE   316 AA;  34701 MW;  95EB96DFAA37C983 CRC64;
     MKIISAEQVH QNLNFEELIP LLKQSFSRPF SMPQRQVYSL APEQSENHDA FALLPSWNEE
     VIGNKAFTYF PDNAKKHDLP GLFSKIMLFK RQTGEPLALV DGTSVTYWRT AAISALASQL
     LSRKNSQHLM LFGTGNLASY LVKAHLTVRD IKQVTLWGRN AKKVSKLIAD FSILYPAVTF
     KTSVDVNAEV ASADIICCAT GAKTPLFDGN SVSAGCHIDC LGNHMTDARE CDTTTILRAR
     VFVDSLTNTL NEAGELLIPM AEDAFNKDEI VGELADMCKT PSMLRQSSDE ITLFKSVGTA
     ISDLVAAHSV VEKLAD